Research workbench
AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine reductase (Q92IT8)
Analyse AlphaFold monomer V2.0 prediction for udp-N- acetylenolpyruvoylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92IT8
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfD2aa30896c43ba48ACc736586610789048c2c7a
- Molecule
- Udp-N-acetylenolpyruvoylglucosamine reductase
- UniProt
- Q92IT8
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylenolpyruvoylglucosamine reductase | protein | 295 | 31% helix, 28% strand | Q92IT8 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 701 | 0.79 | 0.83 | 71 | empty |
| 2 | 61 | 0.32 | 0.76 | 16 | empty |
| 3 | 57 | 0.29 | 0.74 | 16 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q92IT8
- Elsewhere: UniProt Q92IT8 · AlphaFold DB Q92IT8
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